US5858757A - Stabilized enzymes and detergent compositions - Google Patents

Stabilized enzymes and detergent compositions Download PDF

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US5858757A
US5858757A US08/140,083 US14008393A US5858757A US 5858757 A US5858757 A US 5858757A US 14008393 A US14008393 A US 14008393A US 5858757 A US5858757 A US 5858757A
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subtilisin
amino acid
stabilized
protease
bpn
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Claus von der Osten
Sven Branner
Allan Svendsen
Lisbeth Hedegård
Nina Eriksen
Maarten Robert Egmond
Eric Casteleijn
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Novozymes AS
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Novo Nordisk AS
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    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
    • C12N9/52—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea
    • C12N9/54—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea bacteria being Bacillus
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes

Definitions

  • This invention relates to novel stabilized proteases, nucleotide sequences encoding the stabilized proteases, and host organisms containing the nucleotide sequences encoding the novel stabilized proteases.
  • Proteases are enzymes that cleave the amide linkages in protein substrates.
  • Bacteria of the Bacillus species secrete two extracellular species of protease, a neutral or metalloprotease, and an alkaline protease which is functionally a serine endopeptidase, referred to as subtilisin.
  • a serine protease is an enzyme which catalyses the hydrolysis of peptide bonds, and in which there is an essential serine residue at the active site White, Handler and Smith (1973); Principles of Biochemistry; Fifth Edition, McGraw-Hill Book Company, N.Y., 271-272!.
  • the bacterial serine proteases have molecular weights in the range of 20,000 to 45,000. They hydrolyse simple terminal esters and are similar in activity to eukaryotic chymotrypsin, also a serine protease. A more narrow term, alkaline protease, covering a sub-group, reflects the high pH optimum of some of the serine proteases, from pH 9.0 to 11.0 for review, see Priest; Bacteriological Rev., 41 711-753 (1977)!.
  • subtilisin is a serine protease produced by Gram-positive bacteria or fungi.
  • a subtilisin is a serine protease, wherein the relative order of the amino acid residues in the catalytic triad is Asp--His--Ser (positions 32, 64, and 221).
  • Asp--His--Ser positions 32, 64, and 221.
  • subtilisins from Bacillus strains, namely, subtilisin 168, subtilisin BPN', subtilisin Carlsberg, subtilisin DY, subtilisin amylosacchariticus, and mesentericopeptidase Kurihara et al. (1972); J. Biol. Chem.; 247 5629-5631; Wells et al. (1983); Nucleic Acids Res.; 11 7911-7925; Stahl and Ferrari (1984); J. Bacteriol.; 159 811-819; Jacobs et al. (1985); Nucl. Acids Res.; 13 8913-8926; Nedkov et al. (1985); Biol. Chem.
  • protes such as subtilisins have found much utility in industry, particularly in detergent formulations, as they are useful for removing proteinaceous stains.
  • Proteases are globular proteins and quite compact due to the considerable amount of folding of the long polypeptide chain.
  • the polypeptide chain essentially consists of the "backbone” and its “side-groups". As the peptide bond is planar, only rotations around the C a --N axis and the C a --C' axis are permitted. Rotation around the C a --N bond of the peptide backbone is denoted by the torsion angle ⁇ (phi), rotation around the C a --C' bond by ⁇ (psi) vide e.g. Creighton, T. E. (1984); Proteins; W. H. Freeman and Company, New York!.
  • angles of rotation are made by assigning the maximum value of +180° (which is identical to -180°) to the maximally extended chain.
  • the N, C a and C' atoms are all "trans" to each other.
  • the angles ⁇ and ⁇ are assigned the value of 0°. Rotation from this position around the bonds so that the atoms viewed behind the rotated bond move "counter-clockwise” is assigned negative values by definition, those "clockwise” are assigned positive values.
  • the values of the torsion angles lie within the range -180° to +180°.
  • the term "conformation” defines the participation of the secondary and tertiary structures of the polypeptide chains in moulding the overall structure of a protein.
  • the correct conformation of a protein is of prime importance to the specific structure of a protein and contributes greatly to the unique catalytic properties (i.e. activity and specificity) of enzymes and their stability.
  • the amino acids of polypeptides can be divided into four general groups: nonpolar, uncharged polar, and negatively or positively charged polar amino acids.
  • a protein molecule when submerged in its aqueous environment in which it normally occurs, tends to expose a maximum number of its polar side-groups to the surrounding environment, while a majority of its nonpolar side groups is oriented internally. Orientation of the side-groups in this manner leads to a stabilization of protein conformation.
  • Proteins thus, exist in a dynamic equilibrium between a folded and ordered state, and an unfolded and disordered state. This equilibrium in part reflects the short range interactions among the different segments of the polypeptide chain, which tends to stabilize the overall structure of proteins. Thermodynamic forces simultaneously tend to promote randomization of the unfolding molecule.
  • a way to engineer stabilized proteins is to reduce the extent of unfolding by decreasing the flexibility of the polypeptide backbone, and simultaneously decreasing the entropy of the unfolded chain. So far only few attempts have been made to implement this rationale in the development of novel stabilized proteases.
  • thermostability of a globular protein can be enhanced cumulatively to a great extent by increasing the frequency of proline occurrence at the second site of ⁇ -turns without significant alterations in the secondary and tertiary structures as well as in the catalytic function of enzymes.
  • the principle is based on various facts and findings, among these the fact that proline residues show a strong tendency to occur preferentially at the second site of ⁇ -turns Levitt, M (1978); Biochemistry; 17 4277-4285; and Chou, P. Y. & Fasman, G. D. (1977); J. Mol. Biol.; 115 135-175!.
  • the principle is restricted to insertion of proline into the second site of ⁇ -turns in proteins, no other sites are mentioned.
  • the present invention provides novel stabilized proteases, in which a naturally occurring amino acid residue (other than proline) has been substituted with a proline residue at one or more positions, at which position(s) the dihedral angles ⁇ (phi) and ⁇ (psi) constitute values within the intervals -90° ⁇ -40° and -180° ⁇ 180°!, preferably within the intervals -90° ⁇ -40° and 120° ⁇ 180°! or -90° ⁇ -40° and -50° ⁇ 10°!, and which position(s) is/are not located in regions, in which the protease is characterized by possessing ⁇ -helical or, ⁇ -sheet structure.
  • the invention relates to nucleotide sequences encoding the proteases.
  • the invention relates to an expression vector comprising a nucleotide sequence encoding a protease, and to a host organism containing this expression vector.
  • subtilisin is defined as a serine protease produced by gram-positive bacteria or fungi. According to another definition, a subtilisin is a serine protease, wherein the relative order of the amino acid residues in the catalytic triad is Asp--His--Ser (positions 32, 64, and 221, BPN' numbering).
  • a stabilized protease of this invention is a protease variant or mutated protease.
  • a protease variant or mutated protease is meant a protease obtainable by alteration of a DNA nucleotide sequence of the parent gene or its derivatives.
  • the protease variant or mutated protease may be expressed and produced when the DNA nucleotide sequence encoding the protease is inserted into a suitable vector in a suitable host organism.
  • the host organism is not necessarily identical to the organism from which the parent gene originated.
  • subtilisins In the context of this invention a specific numbering of amino acid residue positions in subtilisins is employed. By alignment of the amino acid sequences of various subtilisins along with subtilisin BPN', it is possible to allot a number to the amino acid residue position in any subtilisin to the number of the analogous amino acid position in subtilisin BPN' ("BPN' numbering", vide e.g. International Patent Publications Nos. WO 89/06279 and WO 91/00345).
  • Deletion of an aspartic acid at position 36 is indicated as: D36*, and an insertion in such a position is indicated as: 36D for insertion of an aspartic acid in position 36.
  • subtilisin 309 If a substitution is made by mutation in e.g. subtilisin 309, the product is designated e.g. "subtilisin 309/G195E".
  • proteolytic activity is expressed in Kilo NOVO Protease Units (KNPU).
  • KNPU Kilo NOVO Protease Units
  • the activity is determined relatively to an enzyme standard (SAVINASETM), and the determination is based on the digestion of a dimethyl casein (DMC) solution by the proteolytic enzyme at standard conditions, i.e. 50° C., pH 8.3, 9 min. reaction time, 3 min. measuring time.
  • DMC dimethyl casein
  • a folder AF 220/1 is available upon request to Novo Nordisk A/S, Denmark, which folder is hereby included by reference.
  • wash performance The ability of an enzyme to catalyse the degradation of various naturally occurring substrates present on the objects to be cleaned during e.g. wash is often referred to as its washing ability, washability, detergency, or wash performance. Throughout this application the term wash performance will be used to encompass this property.
  • FIG. 1 shows the construction of a synthetic gene
  • FIG. 2 shows the residual activity of subtilisin 309 variants compared to wild type enzyme after storage in a liquid detergent.
  • the present invention provides novel stabilized proteases, in which a naturally occurring amino acid residue (other than proline) has been substituted with a proline residue at one or more positions, at which position(s) the dihedral angles ⁇ (phi) and ⁇ (psi) constitute values in the intervals -90° ⁇ -40° and -180° ⁇ 180°!, preferably the intervals -90° ⁇ -40° and 120° ⁇ 180°! or -90° ⁇ -40° and -50° ⁇ 10°!, and which position(s) is/are not located in regions, in which the protease is characterized by possessing ⁇ -helical or ⁇ -sheet structure.
  • a stabilized protease is a protease variant or mutated protease, being functionally equivalent or having structural features similar to a naturally occurring protease, and in which protease a naturally occurring amino acid residue (other than proline) has been substituted with a proline residue at one or more positions, at which position(s) the dihedral angles ⁇ (phi) and ⁇ (psi) constitute values within the intervals -90° ⁇ -40° and -180° ⁇ 180°!, preferably the intervals -90° ⁇ -40° and 120° ⁇ 180°! or -90° ⁇ -40° and -50° ⁇ 10°!, and which position(s) is/are not located in regions, in which the protease is characterized by possessing ⁇ -helical or ⁇ -sheet structure.
  • a stabilized protease is a protease having improved stability, e.g. in respect to thermal stability, storage stability, etc., when compared to the parent enzyme.
  • the stabilized proteases of the invention may be obtained by subjecting the protease in question to analysis for secondary structure, identifying residues in the protease having dihedral angles ⁇ (phi) and ⁇ (psi) confined to the intervals -90° ⁇ -40° and -180° ⁇ 180°!, preferably the intervals -90° ⁇ -40° and 120° ⁇ 180°!
  • protease is characterized by possessing ⁇ -helical or ⁇ -sheet structure, if a proline residue is not already at the identified position(s), substitution of the naturally occurring amino acid residue with a proline residue at the identified position(s), preferably by site directed mutagenesis applied on a gene encoding the protease in question, and gene expression by insertion of the gene encoding the stabilized protease in a suitable host organism, followed by cultivation of said host organism in a suitable nutrient medium, and recovery of the desired protease.
  • This preparation includes subjecting the protease in question to analysis for secondary structure.
  • the atomic structure of the protease has to be elucidated.
  • the atomic structure can be determined by X-ray diffraction techniques. X-ray diffraction techniques are described by e.g. Hendrickson, W. A. X-ray diffraction; in Protein Engineering (Ed: Oxender, D. L. and Fox, C. F.), ch. 1; Alan R. Liss, Inc. (1987)! and Creighton, T. E., supra, ch. 6.
  • Subtilisin 309 has been deduced vide Beizel, B., Klupsch, S., Papendorf, G., Hastrup, S., Branner, S., and Wilson, K.S. (1992); J. Mol. Biol. 223 427-445!, and the coordinates have been deposited and are available from the Brookhaven Protein Data Bank Bemstein et al. (1977); J. Mol. Biol. 112 535-542!.
  • the secondary structure elements are defined on the basis of hydrogen bindings. Cooperative secondary structure is recognized as repeats of the elementary hydrogen-bonding patterns "turn” and “bridge”. Repeating turns are “helices”, repeating bridges are “ladders”, connected ladders are “sheets”.
  • a computer program DSSP (Define Secondary Structure of Proteins), enabling the computation of Kabsch & Sander files and written in standard PASCAL, is available from the Protein Data Bank, Chemistry Dept., Brookhaven National Laboratory, Upton, N.Y. 11973.
  • prolines are generally not compatible with ⁇ -helical and ⁇ -sheet secondary conformations. Due to the same rotational constraint about the C a --N bond, and due to the requirement that neighbouring amino acids in the chain are not perturbed, the magnitudes of the dihedral angles phi and psi (and in particular phi) are confined to limited intervals for proline residues in polypeptides.
  • the dihedral angles for proline residues in polypeptides are almost exclusively within the intervals -90° ⁇ -40° and -180° ⁇ 180°!, preferably the intervals -90° ⁇ -40° and 120° ⁇ 180°! or -90° ⁇ -40° and -50° ⁇ 10°!. In this context, both cis- and trans-proline residues are considered.
  • a proline residue may already occur at one or more positions pointed out by the procedure described above, and then a substitution is, of course, irrelevant. Otherwise, the method includes substitution of the naturally occurring amino acid residue with a proline residue.
  • subtilisin different from subtilisin 309 is subjected to this method (although the two subtilisins may seem very much similar), not necessarily the same number of positions, nor particularly the identical positions, may result from the method. It is likely that some of the positions may be identical, and it is likely that the numbers of positions are of equal magnitude, but it is not to be foreseen.
  • Table 1 depicts a set of positions that--with respect to phi and psi angles--meet one criterion
  • Table 2 depicts an additional set of positions that meet another criterion.
  • a protease of the invention is a stabilized subtilisin protease.
  • a preferred protease of the invention is a subtilisin, in which the stabilized subtilisin obtained is any subtilisin which comprises a substitution into a proline residue at one or more of the positions listed in Tables 1 and 2 (BPN' numbers), or positions analogous hereto.
  • a proteases of the invention is a subtilisin in which a naturally occurring amino acid (other than proline) has been substituted with a proline residue at one or more of the positions: 38, 57, 98, 172, 188, 194, 242, and 259 (BPN' numbers).
  • the subtilisin in addition comprises one or more of the following substitutions: 27R, 36D, 76D, 97N, 98R, 104Y, 120D, 128G, 195E, 206C, 218S, 235L, 235R, 237R, 251E, and 263F (BPN' numbers).
  • the protease of the invention is a stabilized subtilisin 309, a stabilized subtilisin 147, a stabilized subtilisin BPN', or a stabilized subtilisin Carlsberg.
  • Subtilisin 309 and Subtilisin 147 are variants of Bacillus lentus and described in U.S. Pat. No. 3,723,250 and International Patent Application PCT/DK88/00002,
  • Subtilisin BPN' is described by Wells et al. Nucleic Acids Res. (1983) 11 7911-7925!;
  • Subtilisin Carlsberg is described by Smith et al. Smith, E. L.; DeLange, R. J.; Evans, W.
  • a protease of the invention is a stabilized subtilisin 309 in which one or more of the following substitutions have been introduced: T38P, S57P, A98P, S188P, A172P, A194P, S242P, and S259P (BPN' numbers).
  • this subtilisin in addition comprises one or more of the following substitutions: K27R, *36D, N76D, G97N, A98R, V104Y, H1 20D, S128G, G195E, Q206C, N218S, K235L, K235R, K237R, K251E, and Y263F (BPN' numbers).
  • the protease of the invention is a subtilisin 309, in which one or more of the following substitutions have been introduced: T38P, S57P, A98P, A172P, A194P, S242P, and S259P (BPN' numbers).
  • this subtilisin 309 in addition comprises one or more of the following substitutions: K27R, *36D, N76D, G97N, A98R, V104Y, H120D, S128G, G195E, Q206C, N218S, K235L, K235R, K237R, K251E, and Y263F (BPN' numbers).
  • proteases of the invention are: Subtilisin 309/K27R+*36D+G97N+A98R+A194P+K235R+K237R+K251E+Y263F, Subtilisin 309/K27R+*36D+G97N+A194P+K235R+K237R+K251E+Y263F, Subtilisin 309/K27R+*36D+G97N+A194P+K235R+K237R+Y263F, Subtilisin 309/*36D+N76D+H120D+A194P+G195E+K235L, Subtilisin 309/*36D+G97N+V104Y+H120D+A194P+G195E, Subtilisin 309/*36D+G97N+V104Y+H120D+A194P+G195E, Subtilisin 309/*36D+G97N+
  • the purified variants obtained according to this invention have been tested to wash at least equally well compared to the wild-type subtilisin (subtilisin 309), vide Example 5 for experimental data.
  • the storage stability generally reflects the thermostability, i.e. improved thermostability corresponds with improved storage stability.
  • the improvement in thermostability of purified variants has been tested by a differential scanning calorimetry (DSC) method, vide Example 3 for experimental data. The result of these tests is shown in Table 3, below.
  • the storage stability has been tested by a Mini Storage Test, vide Example 4 for experimental data, and the results of the storage stability test are shown in FIG. 2.
  • thermostability 2 of the variants possess only slightly improved thermostability
  • 4 of the variants possess no significant change in thermostability
  • 3 of the variants posses significantly decreased thermostability, when compared to the wild-type enzyme.
  • stabilized protease variants which, further to the stabilizing proline residue(s) inserted, contain one or more additional stabilizing mutations as described in this specification, are considered within the scope of this invention.
  • subtilisin genes Many methods for introducing mutations into genes are well known in the art. After a brief discussion of cloning subtilisin genes, methods for generating mutations at specific sites within the subtilisin gene will be discussed.
  • subtilisin may be cloned from any Gram-positive bacteria or fungus by various methods, well known in the art. First a genomic, and/or cDNA library of DNA must be constructed using chromosomal DNA or messenger RNA from the organism that produces the subtilisin to be studied. Then, if the amino-acid sequence of the subtilisin is known, homologous, oligonucleotide probes may be synthesized, labelled, and used to identify subtilisin-encoding clones from a genomic library of bacterial DNA, or from a fungal cDNA library.
  • a labelled oligonucleotide probe containing sequences homologous to subtilisin from another strain of bacteria or fungus could be used as a probe to identify subtilisin-encoding clones, using hybridization and washing conditions of lower stringency.
  • subtilisin-producing clones would involve inserting fragments of genomic DNA into an expression vector, such as a plasmid, transforming protease-negative bacteria with the resulting genomic DNA library, and then plating the transformed bacteria onto agar containing a substrate for subtilisin, such as skim-milk. Those bacteria containing subtilisin-bearing plasmid will produce colonies surrounded by a halo of clear agar, due to digestion of the skim-milk by excreted subtilisin.
  • an expression vector such as a plasmid
  • transforming protease-negative bacteria with the resulting genomic DNA library
  • the mutations can be introduced using synthetic oligonucleotides. These oligonucleotides contain nucleotide sequences flanking the desired mutation sites, mutant nucleotides are inserted during oligonucleotide synthesis.
  • a single stranded gap of DNA, bridging the subtilisin gene is created in a vector bearing the subtilisin gene. Then the synthetic nucleotide, bearing the desired mutation, is annealed to a homologous portion of the single-stranded DNA.
  • the remaining gap is then filled in by DNA polymerase I (Klenow fragment) and the construct is ligated using T4 ligase.
  • DNA polymerase I Klenow fragment
  • T4 ligase A specific example of this method is described Morinaga et al. (1984); Biotechnology, 2 646-639!.
  • Morinaga et al. a fragment within the gene is removed using restriction endonuclease.
  • the vector/gene, now containing a gap is then denatured and hybridized to a vector/gene which, instead of containing a gap, has been cleaved with another restriction endonuclease at a site outside the area involved in the gap.
  • a single-stranded region of the gene is then available for hybridization with mutated oligonucleotides, the remaining gap is filled in by the Klenow fragment of DNA polymerase I, the insertions are ligated with T4 DNA ligase, and, after one cycle of replication, a double-stranded plasmid bearing the desired mutation is produced.
  • the Morinaga method obviates the additional manipulation of constructing new restriction sites, and, therefore, facilitates the generation of mutations at multiple sites.
  • a mutated subtilisin gene produced by methods described above, by the method described in Example 1, or any alternative methods known in the art can be expressed, in enzyme form, using an expression vector.
  • An expression vector generally falls under the definition of a cloning vector, since an expression vector usually includes the components of a typical cloning vector, namely, an element that permits autonomous replication of the vector in a microorganism independent of the genome of the microorganism, and one or more phenotypic markers for selection purposes.
  • An expression vector includes control sequences encoding a promoter, operator, ribosome binding site, translation initiation signal, and, optionally, a repressor gene or various activator genes.
  • nucleotides encoding a "signal sequence" may be inserted prior to the coding sequence of the gene.
  • a target gene to be treated according to the invention is operably linked to the control sequences in the proper reading frame.
  • Promoter sequences that can be incorporated into plasmid vectors, and which can support the transcription of the mutant subtilisin gene include but are not limited to the prokaryotic B-lactamase promoter Villa-Kamaroff, et al. (1978); Proc. Natl. Acad. Sci. U.S.A.; 75 3727-3731! and the tac promoter DeBoer, et al. (1983); Proc. NatI. Acad. Sci. U.S.A.; 80 21-25!. Further references can also be found in "Useful proteins from recombinant bacteria" in Scientific American (1980); 242 74-94.
  • B. subtilis is transformed by an expression vector carrying the mutated DNA. If expression is to take place in a secreting microorganism such as B. subtilis a signal sequence may follow the translation initiation signal and precede the DNA sequence of interest. The signal sequence acts to transport the expression product to the cell wall where it is cleaved from the product upon secretion.
  • control sequences as defined above is intended to include a signal sequence, when it is present.
  • microorganisms able to produce a stabilized enzyme of this invention can be cultivated by conventional fermentation methods in a nutrient medium containing assimilable carbon and nitrogen together with other essential nutrients, the medium being composed in accordance with the principles of the known art.
  • This invention also relates to DNA nucleotide sequences encoding a stabilized protease of the invention, and to an expression vector containing a DNA nucleotide sequence encoding a stabilized protease.
  • the stabilized protease may be expressed and produced when DNA nucleotide sequence encoding this protease is inserted into a suitable expression vector in a suitable host organism.
  • the host organism is not necessarily identical to the organism from which the parent gene originated.
  • the construction of the mutated genes, vectors and mutant and transformed microorganisms may be carried out by any appropriate recombinant DNA technique, known in the art.
  • the invention also relates to host organisms containing an expression vector carrying a DNA nucleotide sequence encoding a stabilized protease.
  • the present invention also comprises the use of the stabilized proteases of the invention in cleaning and detergent compositions and such composition comprising the stabilized proteases.
  • compositions comprise any one or more of the proteases of the invention alone or in combination with any of the usual components included in such compositions which are well-known to the person skilled in the art.
  • Such components comprise builders, such as phosphate or zeolite builders, surfactants, such as anionic, cationic, non-ionic or zwitterionic type surfactants, polymers, such as acrylic or equivalent polymers, bleach systems, such as perborate- or amino-containing bleach precursors or activators, structurants, such as silicate structurants, alkali or acid to adjust pH, humectants, and/or neutral inorganic salts.
  • builders such as phosphate or zeolite builders
  • surfactants such as anionic, cationic, non-ionic or zwitterionic type surfactants
  • polymers such as acrylic or equivalent polymers
  • bleach systems such as perborate- or amino-containing bleach precursors or activators
  • structurants such as silicate structurants, alkali or acid to adjust pH, humectants, and/or neutral inorganic salts.
  • the detergent compositions of the invention can be formulated in any convenient form such as powders, liquids, etc.
  • the enzymes can be used in well-known standard amounts in detergent compositions.
  • the amounts may range very widely, e.g. about 0.0002-0.01, e.g. about 0.005-0.05, Anson units per gram of the detergent composition.
  • the protease can be included in the compositions in amounts in the order of from about 0.1 to 100 GU/mg (e.g. 1-50, especially 5-20 GU/mg) of the detergent formulation, or any amount in a wide range centering at about 0.01-4, e.g. 0.1-0.4 KNPU per g of detergent formulation.
  • a GU is a Glycine Unit, defined as the proteolytic enzyme activity which, under standard conditions, during a 15-minutes' incubation at 40 deg C., with N-acetyl casein as substrate, produces an amount of NH2-group equivalent to 1 micromole of glycine.
  • the present enzymes may for example be suitable to use the present enzymes at the rate of about 0.25 mg of enzyme protein per liter of wash liquor, corresponding to an enzyme activity of the order of 0.08 KNPU per liter.
  • Corresponding detergent formulations can contain the enzymes in for example an amount of the order of 0.1-0.4 KNPU/g.
  • the detergent compositions may also contain further enzymes.
  • lipase can usefully be added in the form of a granular composition (alternatively a solution or a slurry) of lipolytic enzyme with carrier material (e.g. as in EP Patent Publication No. 258,068 (Novo Nordisk ANS) and the LipolaseTM and other enzyme compositions of Novo Nordisk A/S).
  • carrier material e.g. as in EP Patent Publication No. 258,068 (Novo Nordisk ANS) and the LipolaseTM and other enzyme compositions of Novo Nordisk A/S.
  • the added amount of lipase can be chosen within wide limits, for example 50 to 30,000 LU/g per gram of the surfactant system or of the detergent composition, e.g. often at least 100 LU/g, very usefully at least 500 LU/g, sometimes preferably above 1000, above 2000 LU/g or above 4000 LU/g or more, thus very often within the range of 50-4000 LU/g, and possibly within the range of 200-1000 LU/g.
  • lipase units are defined as they are in EP Patent Publication No. 258,068.
  • the lipolytic enzyme can be chosen among a wide range of lipases.
  • lipases showing immunological cross-reactivity with antisera raised against lipase from Chromobacter viscosum var lipolyticum NRRL B-3673, or against lipase from Alcaligenes PL-679, ATCC 31371 and FERM-P 3783, also the lipases described in specifications WO 87/00859 (Gist-Brocades) and EP Patent Publication No. 204,284 (Sapporo Breweries).
  • Suitable, in particular, are for example the following commercially available lipase preparations: Lipolase Novo Nordisk ANS, Amano lipases CE, P, B, AP, M-AP, AML, and CES, and Meito lipases MY-30, OF, and PL, also Esterase MM, Lipozym, SP225, SP285, Saiken lipase, Enzeco lipase, Toyo Jozo lipase and Diosynth lipase (Trade Marks).
  • Amylase can for example be used when desired, in an amount in the range of about 1 to about 100 MU (maltose units) per gram of detergent composition (or 0.014-1.4, e.g. 0.07-0.7, KNU/g (Novo units)).
  • Cellulase can for example be used when desired, in an amount in the range of about 0.3 to about 35 CEVU units per gram of the detergent composition.
  • the compositions may be built or unbuilt, and may be of the zero-P type (i.e. not containing any phosphorus containing builders).
  • the composition may contain in the aggregate for example from 1-50%, e.g. at least about 5% and often up to about 35-40% by weight, of one or more organic and/or inorganic builders.
  • Typical examples of builders include those already mentioned above, and more broadly include alkali metal ortho, pyro, and tripolyphosphates, alkali metal carbonates, either alone or in admixture with calcite, alkali metal citrates, alkali metal nitrilotriacetates, carboxymethyloxysuccinates, zeolites, polyacetalcarboxylates, and so on.
  • the detergent compositions may contain from 1-35% of a bleaching agent or a bleach precursor or a system comprising bleaching agent and/or precursor with activator therefor.
  • Further optional ingredients are lather boosters, foam depressors, anti-corrosion agents, soil-suspending agents, sequestering agents, anti-soil redeposition agents, perfumes, dyes, stabilising agents for the enzymes, and so on.
  • compositions can be used for the washing of textile materials, especially, but without limitation cotton and polyesterbased textiles and mixtures thereof.
  • washing processes carried out at temperatures of about 60°-65° C. or lower, e.g. about 30°-35° C. or lower are particularly suitable.
  • a use-rate from about 1 to 10 g/l, e.g. from about 3-6 g/l, of the detergent formulation is suitable for use in the case when the formulations are substantially as in the Examples.
  • the detergent compositions can be formulated as follows:
  • the anionic detergent is a mixture of sodium dodecyl-benzene sulphonate, alternatively sodium linear alkyl-benzene-sulphonate, 6% and primary alkyl sulphate of 3%.
  • the nonionic detergent is an ethoxylate of an approx. C13-C15 primary alcohol with 7 ethoxylate residues per mole.
  • the zeolite builder is type A zeolite.
  • the polymer is polyacrylic acid.
  • the perborate bleach precursor is sodium tetraborate tetrahydrate or monohydrate.
  • the activator is tetraacetyl-ethylenediamine.
  • the structurant is sodium silicate.
  • the neutral inorganic salt is sodium sulphate.
  • the pH is adjusted to a value between 9 and 10.
  • the detergent compositions can be formulated as e.g. in International Patent Publications Nos. WO 91/00334, WO 91/00335, and International Patent Application No. PCT/DK91/00399.
  • B. subtilis 309 and 147 are variants of Bacillus lentus, deposited with the NCIB and accorded the accession numbers NCIB 10147 and NCIB 10309, and described in U.S. Pat. No. 3,723,250 incorporated by reference herein.
  • E. coli MC 1000 (M. J. Casadaban and S. N. Cohen (1980); J. Mol. Biol.; 138 179-207), was made r-,m+ by conventional methods and is also described in U.S. patent application Ser. No. 039,298.
  • a vector suited to a synthetic gene coding for subtilisin 309 and its mutants was constructed. It is essentially a pUC19 plasmid C. Yanish-Perron and J. Messing (1985); Gene; 33 103-119!, in which the multiple cloning site has been replaced by a linker containing the restriction sites used to separate the five subfragments constituting the gene. The new linker was inserted into Eco RI--HindIll cut pUC19 thereby destroying these sites. ##
  • a synthetic gene coding for the mature part of subtilisin 309 was constructed as shown by the following description and the diagrams given in FIG. 1 (sheets 1/7 to 7/7) of the accompanying drawings.
  • the structure of the synthetic gene is summarised in sheets 1/7 to 4/7, which also indicate fragments used in the construction. Each subfragment was made from 6 to 12 oligonucleotides.
  • the oligonucleotides were synthesised on an automatic DNA synthesizer using phosphoramidite chemistry on a controlled glass support S. L. Beaucage and M. H. Carruthers (1981); Tetrahedron Letters; 22 1859-1869!.
  • Duplexes (indicated in sheets 1/7 to 4/7) were formed from corresponding pairs of oligonucleotides by heating for 5 min at 90 deg C. followed by cooling to room temperature over a period of 75 min. The duplexes were mixed and treated with T4 DNA ligase.
  • the five subfragments were isolated on a 2% agarose gel and inserted into pSX191. The sequence was verified by dideoxynucleotide sequencing. Fragments A-E were isolated and ligated together with KpnI-BamHI cut pSX191. The ligation mixtures were used to transform competent E coli MC1000 r-,m+ selecting for ampicillin resistance. The 850 bp KpnI-BamHI fragment that constitutes the part of the subtilisin 309 gene coding for the mature part of the enzyme was then used to replace the wild type gene on pSX212 giving rise to pSX222, which was then transformed into competent B subtilis SHa273. After fermentation of the transformed strain and purification of the enzyme it was shown that the product was indistinguishable from the wild type product.
  • Protease variants derived from the synthetic gene are made by using oligonucleotides with altered sequence at the place(s) where mutation is wanted (e.g. with sequences as given below) and mixing them with the rest of the oligonucleotides appropriate to the synthetic gene. Assembly of the variant gene is carried out with the variant materials in a manner otherwise analogous to that described above. Further information on synthetic genes generally is available in Agarval et al (1970); Nature; 227 27-34.
  • a KpnI site was introduced into the beginning of the subtilisin 309 synthetic gene encoding the mature part of the enzyme.
  • the method used is called oligonucleotide directed double-strand break repair mutagenesis and is described by Wlodek Mandecki (1986); Proc. Nat. Acad. Sci. USA; 83 7177-7181.
  • pSX1 72 is opened with NcoI at the beginning of the mature part of the subtilisin 309 gene and is mixed with the oligonucleotide NOR 789 (sequence shown in FIG. 1 (7/7)), heated to 100 deg C., cooled to 0 deg C., and transformed into E coli.
  • the recombinants can be screened by colony hybridisation using 32-P-labelled NOR 789.
  • the recombinants that turned out to be positive during the screening had the KpnI site introduced right in front of NcoI by changing two bases without changing the amino acid sequence.
  • pSX172 is described in EP Patent Publication No. 405,901.
  • the KpnI site so created is inserted into pSX120 on a 400-bp PvuI-NheI fragment, giving rise to pSX212.
  • pSX120 is also described in EP Patent Publication No. 405,901.
  • the synthetic gene is inserted between KpnI and BamHI on pSX212, giving rise to pSX222.
  • oligonucleotides were combined with the rest of the oligonucleotides from the synthetic gene that was not changed.
  • This procedure relates to purification of a 10 liter scale fermentation of the Subtilisin 147 enzyme, the Subtilisin 309 enzyme or mutants thereof.
  • the filtrates were concentrated to approximately 400 ml using an Amicon CH2A UF unit equipped with an Amicon S1Y10 UF cartridge.
  • the UF concentrate was centrifuged and filtered prior to absorption at room temperature on a Bacitracin affinity column at pH 7.
  • the protease was eluted from the Bacitracin column at room temperature using 25% 2-propanol and 1M sodium chloride in a buffer solution with 0.01 dimethylglutaric acid, 0.1M boric acid and 0.002M calcium chloride adjusted to pH 7.
  • the fractions with protease activity from the Bacitracin purification step were combined and applied to a 750 ml Sephadex G25 column (5 cm dia.) equilibrated with a buffer containing 0.01 dimethylglutaric acid, 0.2M boric acid and 0.002 m calcium chloride adjusted to pH 6.5.
  • the protease was eluted using a linear gradient of 0-0.1M sodium chloride in 2 liters of the same buffer (0-0.2M sodium chloride in case of sub 147).
  • protease containing fractions from the CM Sepharose column were combined and concentrated in an Amicon ultrafiltration cell equipped with a GR81PP membrane (from the Danish Sugar Factories Inc.).
  • the purified protease variants were subjected to thermal analysis by Differential Scanning Calorimetry (DSC).
  • the instrument was a Setaram micro DSC apparatus connected to HP86 computer for data collection and analysis. Setaram software was used.
  • the enzyme was diluted to a concentration of preferably 2 mg/ml in a liquid built detergent (pH 8.5) of the following composition:
  • the heating rate was 0.5° C./min from 25° C. to 90° C.
  • the storage stability of the enzymes of the invention was determined and compared to the storage stability of subtilisin 309 (wild-type). This stability test is performed as a Mini Storage Test. In each tube 100 ⁇ l of sample were used.
  • the enzyme dosages were 0.25 mg enzyme/g detergent.
  • a liquid detergent composition was used in this test, vide Detergent II, supra.
  • the tubes were incubated at 35° C. for 3, 7, 14, and 21 days, respectively, and the residual activity determined.
  • the residual activity determination method was based on the digestion of a dimethyl casein (DMC) solution by the proteolytic enzymes.
  • DMC dimethyl casein
  • TNBS trinitrobenzene sulphonic acid
  • the activity is determined relative to a sample which immediately after preparation is frozen and kept at a temperature of -10° C. until analysis.
  • the activity of this sample is set to 100%.
  • the activity of the corresponding samples from the storage test is determined relative to the 100% sample.
  • reaction conditions were:
  • thermostability as determined by DSC and storage stability correlate well.
  • the wash performance tests were accomplished on grass juice soiled cotton in a model wash at 20° C., isothermically for 10 minutes.
  • Tests were performed at enzyme concentrations of: 0, 0.025, 0.05, 0.1, 0.5, 1.0, and 2.0 mg enzyme protein/I. Two independent sets of tests were performed for each of the enzymes. The results shown in Tables 5-6 are means of these tests.
  • the protease performance was determined by the change ( ⁇ R) of the remission (% R) at 460 nm measured on a Datacolor Elrephometer 2000, ⁇ R being the remission after wash with protease added minus the remission after wash with no protease added.

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Cited By (42)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US6017871A (en) * 1993-10-14 2000-01-25 The Procter & Gamble Company Protease-containing cleaning compositions
US20040132039A1 (en) * 2001-03-12 2004-07-08 Soren Kjaerulf Screening method comprising combination of discrete dimension assay testing of actives, gene mutation and application assay testing of selected actives
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US20050003985A1 (en) * 2001-10-31 2005-01-06 Beatrix Kottwitz Alkaline protease variants
US20050003504A1 (en) * 2001-12-20 2005-01-06 Angrit Weber Alkaline protease from Bacillus gibsonii (DSM 14391) and washing and cleaning products comprising said alkaline protease
US20050003986A1 (en) * 1988-01-07 2005-01-06 Novozymes A/S Useful mutations of bacterial alkaline protease
US20050009167A1 (en) * 2001-12-22 2005-01-13 Angrit Weber Alkaline protease from Bacillus sp. (DSM 14390) and washing and cleaning products comprising said alkaline protease
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US20050113273A1 (en) * 2001-12-20 2005-05-26 Angrit Weber Alkaline protease from bacillus gibsonii (DSM 14393) and washing and cleaning products comprising said alkaline protease
US20060073559A1 (en) * 2002-03-29 2006-04-06 Eugenio Ferrari Ehanced protein expression in bacillus
US20070270574A1 (en) * 2000-04-03 2007-11-22 Novozymes A/S Subtilisin variants
US20080090745A1 (en) * 2006-10-13 2008-04-17 Fox Bryan P Expression of Streptomyces subtilism inhibitor (SSI) proteins in Bacillus and Streptomyces sp.
US20090011463A1 (en) * 2004-04-09 2009-01-08 Walter Weyler Pcka Modifications and Enhanced Protein Expression in Bacillus
US20090075332A1 (en) * 2007-03-12 2009-03-19 Eugenio Ferrari Modified Proteases
US20090093391A1 (en) * 2007-10-04 2009-04-09 Lanxess Deutschland Gmbh Liquid washing compositions and liquid cleaning compositions
US20090099056A1 (en) * 1997-08-29 2009-04-16 Novozymes A/S Protease Variants and Compositions
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US20090217464A1 (en) * 2008-02-29 2009-09-03 Philip Frank Souter Detergent composition comprising lipase
US20090217463A1 (en) * 2008-02-29 2009-09-03 Philip Frank Souter Detergent composition comprising lipase
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US20110009308A1 (en) * 2004-04-02 2011-01-13 Novozymes A/S Subtilase Variants Having Altered Immunogenicity
US20110229938A1 (en) * 2008-03-28 2011-09-22 Eugenio Ferrari Method For Amplifying Locus In Bacterial Cell
WO2013138288A1 (en) 2012-03-16 2013-09-19 Monosol, Llc. Water soluble compositions incorporating enzymes, and method of making same
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WO2023023644A1 (en) 2021-08-20 2023-02-23 Danisco Us Inc. Polynucleotides encoding novel nucleases, compositions thereof and methods thereof for eliminating dna from protein preparations

Families Citing this family (445)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
DK271490D0 (da) * 1990-11-14 1990-11-14 Novo Nordisk As Detergentkomposition
HUT66846A (en) * 1991-10-16 1995-01-30 Unilever Nv Aqueous enzymatic detergent compositions
ATE376061T1 (de) * 1992-07-17 2007-11-15 Genencor Int Hochalkalische serinproteasen
AU2445195A (en) * 1994-05-04 1995-11-29 Novo Nordisk A/S Protease variants
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JP2006517989A (ja) 2003-02-18 2006-08-03 ノボザイムス アクティーゼルスカブ 洗剤組成物
WO2004099228A2 (en) 2003-05-02 2004-11-18 Novozymes Inc. Variants of beta-glucosidases
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CN1902310B (zh) 2003-10-28 2011-09-21 诺维信股份有限公司 具有β-葡糖苷酶活性的多肽和编码所述多肽的多核苷酸
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CN102250861A (zh) 2004-02-13 2011-11-23 诺维信公司 蛋白酶变体
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US8546106B2 (en) 2006-07-21 2013-10-01 Novozymes, Inc. Methods of increasing secretion of polypeptides having biological activity
AU2007284126B2 (en) 2006-08-11 2013-12-19 Novozymes Biologicals, Inc. Bacteria cultures and compositions comprising bacteria cultures
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KR20100014954A (ko) 2007-03-09 2010-02-11 다니스코 유에스 인크. 호알칼리성 바실러스 종 α-아밀라아제 변이체, α-아밀라아제 변이체를 함유하는 조성물 및 사용 방법
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DE102007016139A1 (de) 2007-03-30 2008-10-02 Jenabios Gmbh Verfahren zur regioselektiven Oxygenierung von N-Heterozyklen
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WO2009134670A2 (en) 2008-04-30 2009-11-05 Danisco Us Inc., Genencor Division New chimeric alpha-amylase variants
EP2285944B1 (en) 2008-05-14 2013-03-13 Novozymes A/S Liquid detergent compositions
CN102112621A (zh) 2008-06-06 2011-06-29 丹尼斯科美国公司 用来自枯草芽孢杆菌的α-淀粉酶从淀粉产生葡萄糖
WO2009149283A1 (en) 2008-06-06 2009-12-10 Danisco Us Inc. Saccharification enzyme composition
BRPI0915606A2 (pt) 2008-06-06 2021-03-09 Danisco Us Inc. Alfa-amilases variantes de bacillus subtilis e métodos de uso das mesmas
ES2527645T3 (es) 2008-06-06 2015-01-27 Danisco Us Inc. Variantes de alfa-amilasa de Geobacillus stearothermophilus (AMYS) con propiedades mejoradas
EP2149786A1 (en) 2008-08-01 2010-02-03 Unilever PLC Improvements relating to detergent analysis
DE212009000119U1 (de) 2008-09-12 2011-12-30 Unilever N.V. Spender und Vorbehandlungsmittel für viskose Flüssigkeiten
BRPI0920891B1 (pt) 2008-09-25 2023-01-10 Danisco Us Inc Mistura de alfa-amilase e método para produção de um açúcar fermentável
CN102292444A (zh) 2008-11-20 2011-12-21 诺维信股份有限公司 具有淀粉分解增强活性的多肽和编码该多肽的多核苷酸
WO2010065830A1 (en) 2008-12-04 2010-06-10 Novozymes, Inc. Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same
EP2376527A1 (en) 2008-12-12 2011-10-19 Novozymes Inc. Polypeptides having lipase activity and polynucleotides encoding same
EP2202290A1 (en) 2008-12-23 2010-06-30 Unilever PLC A flowable laundry composition and packaging therefor
EP2401371A1 (en) 2009-02-27 2012-01-04 Novozymes A/S Mutant cells having reduced expression of metallopeptidase, suitable for recombinant polypeptide production
EP2406373B1 (en) 2009-03-10 2014-05-28 Danisco US Inc. Bacillus megaterium strain dsm90-related alpha-amylases, and methods of use, thereof
MX2011010041A (es) 2009-04-01 2011-11-18 Danisco Us Inc Composiciones y metodos que comprenden variantes de alfa-amilasa con propiedades alteradas.
BRPI1012590A2 (pt) 2009-04-08 2015-09-22 Danisco Us Inc Genencor Div alfa-amilases relacionadas à cepa wdg-195 de halomonas e métodos de uso das mesmas
US8569581B2 (en) 2009-09-17 2013-10-29 Novozymes, Inc Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same
JP6204018B2 (ja) 2009-09-25 2017-09-27 ノボザイムス アクティーゼルスカブ プロテアーゼ変異体の使用
MX339581B (es) 2009-09-25 2016-06-01 Novozymes As Variantes de subtilasa.
MX2012003473A (es) 2009-09-29 2012-05-22 Novozymes Inc Polipeptidos que tienen actividad celulitica mejorada y polinucleotidos que codifican para los mismos.
CA2775244A1 (en) 2009-09-30 2011-04-07 Novozymes A/S Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same
CN102695720B (zh) 2009-09-30 2018-02-16 诺维信股份有限公司 具有纤维素分解增强活性的多肽和编码该多肽的多核苷酸
CA2778471A1 (en) 2009-10-23 2011-04-28 Danisco Us Inc. Methods for reducing blue saccharide
WO2011080267A2 (en) 2009-12-29 2011-07-07 Novozymes A/S Polypetides having detergency enhancing effect
MX2012008389A (es) 2010-01-22 2012-08-15 Dupont Nutrition Biosci Aps Metodos para producir compuestos glicolipidos sustituidos con aminas.
WO2011100667A1 (en) 2010-02-14 2011-08-18 Ls9, Inc. Surfactant and cleaning compositions comprising microbially produced branched fatty alcohols
WO2011102933A1 (en) 2010-02-18 2011-08-25 Danisco Us Inc. Amylase from nesterenkonia and methods of use, thereof
MX2012009705A (es) 2010-02-25 2012-12-17 Novozymes As Variantes de lisozima y polinucleotidos que codifican la misma.
WO2011120882A1 (en) 2010-03-30 2011-10-06 Novozymes A/S Crystal metabolite recovery
EP2563910B1 (en) 2010-04-26 2015-09-30 Novozymes A/S Enzyme granules
BR112012028033B1 (pt) 2010-06-22 2021-04-27 Novozymes A/S Método para desprender pelos em couro cru ou peles, processos para depilação de couro cru ou peles, e, para preparar um azul molhado
MX2013002248A (es) 2010-08-30 2013-05-09 Novozymes As Lavado con remojado concentrado.
BR112013003845A2 (pt) 2010-08-30 2016-07-05 Novozymes As "método de limpeza de objetos com duas imersões"
WO2012035103A1 (en) 2010-09-16 2012-03-22 Novozymes A/S Lysozymes
GB201015672D0 (en) 2010-09-20 2010-10-27 Unilever Plc Improvements relating to fabric treatment compositions comprising targeted benefit agents
DK2622070T3 (en) 2010-09-30 2016-11-21 Novozymes Inc Variants of polypeptides having cellulolytic enhancing ACTIVITY AND POLYNUCLEOTIDES ENCODING THEM
DK2622068T3 (en) 2010-09-30 2016-10-17 Novozymes Inc Variants of polypeptides having cellulolytic enhancing ACTIVITY AND POLYNUCLEOTIDES ENCODING THEM
US9676830B2 (en) 2010-11-18 2017-06-13 Novozymes, Inc. Chimeric polypeptides having cellulolytic enhancing activity and polynucleotides encoding same
US9228284B2 (en) 2011-02-15 2016-01-05 Novozymes North America, Inc. Mitigation of odor in cleaning machines and cleaning processes
US20140038876A1 (en) 2011-02-16 2014-02-06 Novozymes A/S Detergent Compositions Comprising Mettaloproteases
JP2014508830A (ja) 2011-02-16 2014-04-10 ノボザイムス アクティーゼルスカブ 金属プロテアーゼを含む洗剤組成物
CN103502418A (zh) 2011-02-16 2014-01-08 诺维信公司 包含金属蛋白酶的去污剂组合物
GB201102857D0 (en) 2011-02-18 2011-04-06 Danisco Feed additive composition
GB201102865D0 (en) 2011-02-18 2011-04-06 Danisco Feed additive composition
DK2678352T3 (en) 2011-02-23 2018-03-05 Novozymes Inc Polypeptides with cellulolysis enhancing activity and polynucleotides encoding them
WO2012135659A2 (en) 2011-03-31 2012-10-04 Novozymes A/S Methods for enhancing the degradation or conversion of cellulosic material
AU2012241055A1 (en) 2011-04-08 2013-08-15 Danisco Us, Inc. Compositions
US9624518B2 (en) 2011-04-29 2017-04-18 Novozymes, Inc. Methods for enhancing the degradation or conversion of cellulosic material
CN107475235B (zh) 2011-06-20 2022-09-13 诺维信公司 颗粒组合物
EP2537918A1 (en) 2011-06-20 2012-12-26 The Procter & Gamble Company Consumer products with lipase comprising coated particles
JP6126086B2 (ja) 2011-06-24 2017-05-10 ノボザイムス アクティーゼルスカブ プロテアーゼ活性を有するポリペプチドおよびこれをコードするポリヌクレオチド
WO2013001087A2 (en) 2011-06-30 2013-01-03 Novozymes A/S Method for screening alpha-amylases
AU2012277721B2 (en) 2011-06-30 2017-06-22 Novozymes A/S Alpha-amylase variants
EP2726590B1 (en) 2011-07-01 2017-10-18 Novozymes A/S Liquid detergent composition
RU2635355C2 (ru) 2011-07-01 2017-11-13 Новозимс А/С Композиция со стабилизированным субтилизином
EP2732018B1 (en) 2011-07-12 2017-01-04 Novozymes A/S Storage-stable enzyme granules
MX2014001594A (es) 2011-08-15 2014-04-25 Novozymes As Polipeptidos que tienen actividad de celulasa y polinucleotidos que los codifican.
ES2628190T3 (es) 2011-09-22 2017-08-02 Novozymes A/S Polipéptidos con actividad de proteasa y polinucleótidos que codifican los mismos
EP3246404B1 (en) 2011-10-28 2019-02-27 Danisco US Inc. Variant maltohexaose-forming alpha-amylase variants
BR112014012165A2 (pt) 2011-11-21 2020-06-23 Novozymes, Inc. Variante de um polipeptídeo gh61, polinucleotídeo isolado, célula hospedeira recombinante, método para produção de uma variante de um polipeptídeo gh61, processos para degradação ou conversão de um material celulósico, para produção de um produto de fermentação, e para fermentação de um material celulósico, composição enzimática, formulação de caldo completo, ou composição de cultura celular, composição detergente, e método de limpeza ou lavagem de uma superfície dura ou roupa.
ES2631605T3 (es) 2011-11-25 2017-09-01 Novozymes A/S Polipéptidos con actividad de lisozima y polinucleótidos que codifican los mismos
MX2014006205A (es) 2011-11-25 2014-07-14 Novozymes As Variantes de subtilasa y polinucleotidos que las codifican.
EP2791330B1 (en) 2011-12-16 2017-07-26 Novozymes, Inc. Polypeptides having laccase activity and polynucleotides encoding same
JP2015504660A (ja) 2011-12-20 2015-02-16 ノボザイムス アクティーゼルスカブ サブチラーゼ変異体およびそれをコードするポリヌクレオチド
EP2607468A1 (en) 2011-12-20 2013-06-26 Henkel AG & Co. KGaA Detergent compositions comprising subtilase variants
WO2013096653A1 (en) 2011-12-22 2013-06-27 Danisco Us Inc. Compositions and methods comprising a lipolytic enzyme variant
CA2858252A1 (en) 2011-12-22 2013-06-27 Danisco Us Inc. Variant alpha-amylases and methods of use, thereof
JP2015507675A (ja) 2011-12-29 2015-03-12 ノボザイムス アクティーゼルスカブ 洗剤組成物
EP2807254B1 (en) 2012-01-26 2017-08-02 Novozymes A/S Use of polypeptides having protease activity in animal feed and detergents
JP2015509364A (ja) 2012-02-17 2015-03-30 ノボザイムス アクティーゼルスカブ サブチリシン変異体およびそれをコードするポリヌクレオチド
EP2628785B1 (en) 2012-02-17 2016-05-18 Henkel AG & Co. KGaA Detergent compositions comprising subtilase variants
WO2013131964A1 (en) 2012-03-07 2013-09-12 Novozymes A/S Detergent composition and substitution of optical brighteners in detergent compositions
EP2831215B1 (en) 2012-03-29 2018-08-08 Novozymes A/S Use of enzymes for preparing water soluble films
EP2841567B1 (en) 2012-04-27 2017-07-26 Novozymes, Inc. Gh61 polypeptide variants and polynucleotides encoding same
ES2643216T3 (es) 2012-05-07 2017-11-21 Novozymes A/S Polipéptidos con actividad de degradación de xantano y polinucleótidos que codifican la misma
WO2013169645A1 (en) 2012-05-11 2013-11-14 Danisco Us Inc. Use of alpha-amylase from aspergillus clavatus for saccharification
WO2013171241A1 (en) 2012-05-16 2013-11-21 Novozymes A/S Compositions comprising lipase and methods of use thereof
CA2874061A1 (en) 2012-06-08 2014-01-09 Danisco Us Inc. Variant alpha amylases with enhanced activity on starch polymers
US20150184208A1 (en) 2012-06-19 2015-07-02 Novozymes A/S Enzymatic reduction of hydroperoxides
CN104394708A (zh) 2012-06-20 2015-03-04 诺维信公司 具有蛋白酶活性的多肽在动物饲料和洗涤剂中的用途
WO2014026630A1 (en) 2012-08-16 2014-02-20 Novozymes A/S Method for treating textile with endoglucanase
CA2878988A1 (en) 2012-08-16 2014-02-20 Danisco Us Inc. Method of using alpha-amylase from aspergillus clavatus and pullulanase for saccharification
MX2015002211A (es) 2012-08-22 2015-05-08 Novozymes As Metaloproteasa de exiguobacterium.
BR112015003726A2 (pt) 2012-08-22 2019-09-24 Novozymes As composição detergente, uso de uma composição e de um polipeptídeo, e, método para remoção de uma nódoa de uma superfície.
CN104603266B (zh) 2012-08-22 2017-11-10 诺维信公司 来自脂环酸芽孢杆菌属的金属蛋白酶
EP2922951B1 (en) 2012-11-20 2017-08-23 Danisco US Inc. Amylase with maltogenic properties
DK2929004T3 (da) 2012-12-07 2019-07-29 Novozymes As Forebyggelse af bakterieadhæsion
EP2931872B1 (en) 2012-12-11 2018-01-17 Danisco US Inc. Trichoderma reesei host cells expressing a glucoamylase from aspergillus fumigatus and methods of use thereof
CA2894513A1 (en) 2012-12-14 2014-06-19 Danisco Us Inc. Method of using alpha-amylase from aspergillus fumigatus and isoamylase for saccharification
WO2014090940A1 (en) 2012-12-14 2014-06-19 Novozymes A/S Removal of skin-derived body soils
US20160010128A1 (en) 2012-12-20 2016-01-14 Danisco Us Inc. Method of using alpha-amylase from aspergillus terreus and pullulanase for saccharification
EP2934177B1 (en) 2012-12-21 2017-10-25 Novozymes A/S Polypeptides having protease activiy and polynucleotides encoding same
WO2014099525A1 (en) 2012-12-21 2014-06-26 Danisco Us Inc. Paenibacillus curdlanolyticus amylase, and methods of use, thereof
EP2935575B1 (en) 2012-12-21 2018-04-18 Danisco US Inc. Alpha-amylase variants
CN112458069A (zh) 2013-01-03 2021-03-09 诺维信公司 α-淀粉酶变体以及对其进行编码的多核苷酸
WO2014164800A1 (en) 2013-03-11 2014-10-09 Danisco Us Inc. Alpha-amylase combinatorial variants
CN105189724A (zh) 2013-03-14 2015-12-23 诺维信公司 含有酶和抑制剂的水溶性膜
EP2989117B1 (en) 2013-04-23 2019-06-12 Novozymes A/S Liquid automatic dish washing detergent compositions with stabilised subtilisin
WO2014177709A1 (en) 2013-05-03 2014-11-06 Novozymes A/S Microencapsulation of detergent enzymes
RU2712877C2 (ru) 2013-05-14 2020-01-31 Новозимс А/С Моющие композиции
CN105209613A (zh) 2013-05-17 2015-12-30 诺维信公司 具有α淀粉酶活性的多肽
US10538751B2 (en) 2013-06-06 2020-01-21 Novozymes A/S Alpha-amylase variants and polynucleotides encoding same
PE20160799A1 (es) 2013-06-12 2016-09-03 Earth Alive Clean Tech Inc Supresor de polvo
WO2014200658A1 (en) 2013-06-13 2014-12-18 Danisco Us Inc. Alpha-amylase from promicromonospora vindobonensis
WO2014200657A1 (en) 2013-06-13 2014-12-18 Danisco Us Inc. Alpha-amylase from streptomyces xiamenensis
WO2014200656A1 (en) 2013-06-13 2014-12-18 Danisco Us Inc. Alpha-amylase from streptomyces umbrinus
WO2014204596A1 (en) 2013-06-17 2014-12-24 Danisco Us Inc. Alpha-amylase from bacillaceae family member
WO2014207227A1 (en) 2013-06-27 2014-12-31 Novozymes A/S Subtilase variants and polynucleotides encoding same
WO2014207224A1 (en) 2013-06-27 2014-12-31 Novozymes A/S Subtilase variants and polynucleotides encoding same
EP3017032A2 (en) 2013-07-04 2016-05-11 Novozymes A/S Polypeptides having anti-redeposition effect and polynucleotides encoding same
US20160160196A1 (en) 2013-07-09 2016-06-09 Novozymes A/S Polypeptides with Lipase Activity And Polynucleotides Encoding Same
WO2015010009A2 (en) 2013-07-19 2015-01-22 Danisco Us Inc. Compositions and methods comprising a lipolytic enzyme variant
WO2015014803A1 (en) 2013-07-29 2015-02-05 Novozymes A/S Protease variants and polynucleotides encoding same
EP3611260A1 (en) 2013-07-29 2020-02-19 Novozymes A/S Protease variants and polynucleotides encoding same
EP3339436B1 (en) 2013-07-29 2021-03-31 Henkel AG & Co. KGaA Detergent composition comprising protease variants
EP3052622B1 (en) 2013-10-03 2018-09-19 Danisco US Inc. Alpha-amylases from a subset of exiguobacterium, and methods of use, thereof
WO2015050723A1 (en) 2013-10-03 2015-04-09 Danisco Us Inc. Alpha-amylases from exiguobacterium, and methods of use, thereof
WO2015049370A1 (en) 2013-10-03 2015-04-09 Novozymes A/S Detergent composition and use of detergent composition
WO2015077126A1 (en) 2013-11-20 2015-05-28 Danisco Us Inc. Variant alpha-amylases having reduced susceptibility to protease cleavage, and methods of use, thereof
WO2015094809A1 (en) 2013-12-19 2015-06-25 Danisco Us Inc. Chimeric fungal alpha-amylases comprising carbohydrate binding module and the use thereof
CN105814200A (zh) 2013-12-20 2016-07-27 诺维信公司 具有蛋白酶活性的多肽以及编码它们的多核苷酸
US10463701B2 (en) 2013-12-31 2019-11-05 DuPont Nutrition BioScience ApS Blends of Bacillus strains and enzymes
WO2015109972A1 (en) 2014-01-22 2015-07-30 Novozymes A/S Polypeptides with lipase activity and polynucleotides encoding same
WO2015134729A1 (en) 2014-03-05 2015-09-11 Novozymes A/S Compositions and methods for improving properties of non-cellulosic textile materials with xyloglucan endotransglycosylase
CN106062271A (zh) 2014-03-05 2016-10-26 诺维信公司 用于改进具有木葡聚糖内糖基转移酶的纤维素纺织材料的性质的组合物和方法
CN111500552A (zh) 2014-03-12 2020-08-07 诺维信公司 具有脂肪酶活性的多肽和编码它们的多核苷酸
WO2015150457A1 (en) 2014-04-01 2015-10-08 Novozymes A/S Polypeptides having alpha amylase activity
DK3406697T3 (da) 2014-04-11 2020-08-31 Novozymes As Detergentsammensætning
WO2015158237A1 (en) 2014-04-15 2015-10-22 Novozymes A/S Polypeptides with lipase activity and polynucleotides encoding same
EP3149178B1 (en) 2014-05-27 2020-07-15 Novozymes A/S Lipase variants and polynucleotides encoding same
EP3149160B1 (en) 2014-05-27 2021-02-17 Novozymes A/S Methods for producing lipases
US20170121695A1 (en) 2014-06-12 2017-05-04 Novozymes A/S Alpha-amylase variants and polynucleotides encoding same
EP3164476A1 (en) 2014-07-03 2017-05-10 Novozymes A/S Improved stabilization of non-protease enzyme
EP3172329A1 (en) 2014-10-24 2017-05-31 Danisco US Inc. Method for producing alcohol by use of a tripeptidyl peptidase
WO2016079110A2 (en) 2014-11-19 2016-05-26 Novozymes A/S Use of enzyme for cleaning
EP3221447A1 (en) 2014-11-20 2017-09-27 Novozymes A/S Alicyclobacillus variants and polynucleotides encoding same
WO2016087401A1 (en) 2014-12-05 2016-06-09 Novozymes A/S Lipase variants and polynucleotides encoding same
DK3399031T3 (da) 2014-12-15 2020-01-20 Henkel Ag & Co Kgaa Detergentsammensætning med subtilasevarianter
CN107002049A (zh) 2014-12-16 2017-08-01 诺维信公司 具有n‑乙酰基葡萄糖胺氧化酶活性的多肽
ES2813727T3 (es) 2014-12-19 2021-03-24 Novozymes As Variantes de proteasa y polinucleótidos que las codifican
WO2016097352A1 (en) 2014-12-19 2016-06-23 Novozymes A/S Protease variants and polynucleotides encoding same
MX2017012515A (es) 2015-04-06 2018-01-30 Dupont Nutrition Biosci Aps Proteasas para productos lacteos fermentados ricos en proteinas.
CN107567489A (zh) 2015-04-10 2018-01-09 诺维信公司 衣物洗涤方法，dna酶和洗涤剂组合物的用途
EP3280800A1 (en) 2015-04-10 2018-02-14 Novozymes A/S Detergent composition
WO2016184944A1 (en) 2015-05-19 2016-11-24 Novozymes A/S Odor reduction
BR112017025607B1 (pt) 2015-06-02 2022-08-30 Unilever Ip Holdings B.V. Composição de detergente para lavagem de roupas e método doméstico de tratamento de um tecido
EP3101109B1 (en) 2015-06-04 2018-03-07 The Procter and Gamble Company Hand dishwashing liquid detergent composition
EP3101108B1 (en) 2015-06-04 2018-01-31 The Procter and Gamble Company Hand dishwashing liquid detergent composition
CN107690472B (zh) 2015-06-11 2020-10-27 荷兰联合利华有限公司 洗衣洗涤剂组合物
WO2016202739A1 (en) 2015-06-16 2016-12-22 Novozymes A/S Polypeptides with lipase activity and polynucleotides encoding same
CN107922095A (zh) 2015-06-17 2018-04-17 诺维信公司 容器
BR112017027402B1 (pt) 2015-06-26 2022-05-10 Unilever Ip Holdings B.V. Composição de detergente para lavagem de roupas e método de tratamento doméstico de um tecido
US20180171271A1 (en) 2015-06-30 2018-06-21 Novozymes A/S Laundry detergent composition, method for washing and use of composition
EP3929285A3 (en) 2015-07-01 2022-05-25 Novozymes A/S Methods of reducing odor
CN114292829A (zh) 2015-07-06 2022-04-08 诺维信公司 脂肪酶变体以及编码它们的多核苷酸
EP3350323B1 (en) 2015-09-17 2021-04-14 Novozymes A/S Polypeptides having xanthan degrading activity and polynucleotides encoding same
US11053486B2 (en) 2015-09-17 2021-07-06 Henkel Ag & Co. Kgaa Detergent compositions comprising polypeptides having xanthan degrading activity
EP3356504B1 (en) 2015-10-01 2019-08-14 Unilever PLC Powder laundry detergent composition
US10844360B2 (en) 2015-10-07 2020-11-24 Novozymes A/S Polypeptides
CN108291212A (zh) 2015-10-14 2018-07-17 诺维信公司 多肽变体
EP3362558A1 (en) 2015-10-14 2018-08-22 Novozymes A/S Polypeptides having protease activity and polynucleotides encoding same
WO2017066510A1 (en) 2015-10-14 2017-04-20 Novozymes A/S Cleaning of water filtration membranes
US11028346B2 (en) 2015-10-28 2021-06-08 Novozymes A/S Detergent composition comprising protease and amylase variants
KR20180067700A (ko) 2015-11-09 2018-06-20 듀폰 뉴트리션 바이오사이언시즈 에이피에스 사료 첨가제 조성물
EP3380608A1 (en) 2015-11-24 2018-10-03 Novozymes A/S Polypeptides having protease activity and polynucleotides encoding same
CN108431217B (zh) 2015-12-01 2022-06-21 诺维信公司 用于产生脂肪酶的方法
CN108431220B (zh) 2015-12-07 2022-06-07 诺维信公司 具有β-葡聚糖酶活性的多肽、编码其的多核苷酸及其在清洁和洗涤剂组合物中的用途
WO2017097869A1 (en) 2015-12-09 2017-06-15 Basf Se Method of purifying a protein from fermentation solids under desorbing conditions
CN108779448B (zh) 2015-12-09 2023-08-18 丹尼斯科美国公司 α-淀粉酶组合变体
WO2017117089A1 (en) 2015-12-28 2017-07-06 Novozymes Bioag A/S Heat priming of bacterial spores
CA3006607A1 (en) 2015-12-30 2017-07-06 Novozymes A/S Enzyme variants and polynucleotides encoding the same
CA3007148A1 (en) 2016-01-29 2017-08-03 Novozymes A/S Beta-glucanase variants and polynucleotides encoding same
CN108603140B (zh) 2016-02-17 2020-09-08 荷兰联合利华有限公司 增白组合物
BR112018068068B1 (pt) 2016-03-21 2023-04-18 Unilever Ip Holdings B.V. Composição aquosa líquida de detergente para lavagem de roupas e método doméstico de tratamento de um tecido
BR112018069220A2 (pt) 2016-03-23 2019-01-22 Novozymes As uso de polipeptídeo que tem atividade de dnase para tratamento de tecidos
WO2017173190A2 (en) 2016-04-01 2017-10-05 Danisco Us Inc. Alpha-amylases, compositions & methods
WO2017173324A2 (en) 2016-04-01 2017-10-05 Danisco Us Inc. Alpha-amylases, compositions & methods
CN109312270B (zh) 2016-04-08 2022-01-28 诺维信公司 洗涤剂组合物及其用途
CN108779416B (zh) 2016-04-08 2021-01-05 荷兰联合利华有限公司 洗衣洗涤剂组合物
WO2017186943A1 (en) 2016-04-29 2017-11-02 Novozymes A/S Detergent compositions and uses thereof
WO2017191160A1 (en) 2016-05-03 2017-11-09 Novozymes A/S Alpha-amylase variants and polynucleotides encoding the same
US11186833B2 (en) 2016-05-09 2021-11-30 Novozymes A/S Variant polypeptides with improved performance and use of the same
WO2017210188A1 (en) 2016-05-31 2017-12-07 Novozymes A/S Stabilized liquid peroxide compositions
US11001787B2 (en) 2016-06-23 2021-05-11 Novozymes A/S Use of enzymes, composition and method for removing soil
CN117721095A (zh) 2016-06-30 2024-03-19 诺维信公司 脂肪酶变体及包含表面活性剂和脂肪酶变体的组合物
WO2018002261A1 (en) 2016-07-01 2018-01-04 Novozymes A/S Detergent compositions
WO2018007573A1 (en) 2016-07-08 2018-01-11 Novozymes A/S Detergent compositions with galactanase
EP3485010A1 (en) 2016-07-13 2019-05-22 The Procter and Gamble Company Bacillus cibi dnase variants and uses thereof
CN109477065A (zh) 2016-07-14 2019-03-15 巴斯夫欧洲公司 包含螯合剂的发酵培养基
CN109790525A (zh) 2016-07-18 2019-05-21 诺维信公司 脂肪酶变体、编码其的多核苷酸及其用途
MX2019001671A (es) 2016-08-08 2019-07-04 Basf Se Formulacion liquida de lavanderia.
EP3284805B1 (en) 2016-08-17 2020-02-19 The Procter & Gamble Company Cleaning composition comprising enzymes
US10988747B2 (en) 2016-08-24 2021-04-27 Henkel Ag & Co. Kgaa Detergent composition comprising GH9 endoglucanase variants I
AU2017317563B8 (en) 2016-08-24 2023-03-23 Henkel Ag & Co. Kgaa Detergent compositions comprising xanthan lyase variants I
CN109863244B (zh) 2016-08-24 2023-06-06 诺维信公司 Gh9内切葡聚糖酶变体以及编码它们的多核苷酸
CN109844110B (zh) 2016-08-24 2023-06-06 诺维信公司 黄原胶裂解酶变体以及编码它们的多核苷酸
EP3519542B1 (en) 2016-09-27 2020-02-19 Unilever PLC Domestic laundering method
WO2018060475A1 (en) 2016-09-29 2018-04-05 Novozymes A/S Spore containing granule
US20200140786A1 (en) 2016-09-29 2020-05-07 Novozymes A/S Use of enzyme for washing, method for washing and warewashing composition
EP3532592A1 (en) 2016-10-25 2019-09-04 Novozymes A/S Detergent compositions
US11753605B2 (en) 2016-11-01 2023-09-12 Novozymes A/S Multi-core granules
RU2019120191A (ru) 2016-12-01 2021-01-11 Басф Се Стабилизация ферментов в композициях
US20190292493A1 (en) 2016-12-12 2019-09-26 Novozymes A/S Use of polypeptides
EP3555255B1 (en) 2016-12-15 2020-06-24 Unilever PLC Laundry detergent composition
EP3601549A1 (en) 2017-03-31 2020-02-05 Novozymes A/S Polypeptides having dnase activity
US11208639B2 (en) 2017-03-31 2021-12-28 Novozymes A/S Polypeptides having DNase activity
WO2018178061A1 (en) 2017-03-31 2018-10-04 Novozymes A/S Polypeptides having rnase activity
US20200109354A1 (en) 2017-04-04 2020-04-09 Novozymes A/S Polypeptides
CN110651029B (zh) 2017-04-04 2022-02-15 诺维信公司 糖基水解酶
US20200109352A1 (en) 2017-04-04 2020-04-09 Novozymes A/S Polypeptide compositions and uses thereof
EP3385362A1 (en) 2017-04-05 2018-10-10 Henkel AG & Co. KGaA Detergent compositions comprising fungal mannanases
EP3385361B1 (en) 2017-04-05 2019-03-27 Henkel AG & Co. KGaA Detergent compositions comprising bacterial mannanases
CA3058520A1 (en) 2017-04-06 2018-10-11 Novozymes A/S Detergent compositions and uses thereof
WO2018185285A1 (en) 2017-04-06 2018-10-11 Novozymes A/S Cleaning compositions and uses thereof
WO2018184818A1 (en) 2017-04-06 2018-10-11 Novozymes A/S Cleaning compositions and uses thereof
EP3607043A1 (en) 2017-04-06 2020-02-12 Novozymes A/S Cleaning compositions and uses thereof
WO2018185269A1 (en) 2017-04-06 2018-10-11 Novozymes A/S Cleaning compositions and uses thereof
EP3607037A1 (en) 2017-04-06 2020-02-12 Novozymes A/S Cleaning compositions and uses thereof
DK3478811T3 (da) 2017-04-06 2020-01-27 Novozymes As Rengøringssammensætninger og anvendelser deraf
US11078445B2 (en) 2017-05-05 2021-08-03 Novozymes A/S Compositions comprising lipase and sulfite
CA3058095A1 (en) 2017-05-08 2018-11-15 Novozymes A/S Mannanase variants and polynucleotides encoding same
WO2018206300A1 (en) 2017-05-08 2018-11-15 Novozymes A/S Mannanase variants and polynucleotides encoding same
WO2018206535A1 (en) 2017-05-08 2018-11-15 Novozymes A/S Carbohydrate-binding domain and polynucleotides encoding the same
EP3401385A1 (en) 2017-05-08 2018-11-14 Henkel AG & Co. KGaA Detergent composition comprising polypeptide comprising carbohydrate-binding domain
WO2018224544A1 (en) 2017-06-08 2018-12-13 Novozymes A/S Compositions comprising polypeptides having cellulase activity and amylase activity, and uses thereof in cleaning and detergent compositions
EP3645692A1 (en) 2017-06-30 2020-05-06 Novozymes A/S Enzyme slurry composition
WO2019030186A1 (en) 2017-08-07 2019-02-14 Novozymes A/S USING FCA CONTROL BASED ON PH
EP3673056A1 (en) 2017-08-24 2020-07-01 Henkel AG & Co. KGaA Detergent compositions comprising gh9 endoglucanase variants ii
US11525128B2 (en) 2017-08-24 2022-12-13 Novozymes A/S GH9 endoglucanase variants and polynucleotides encoding same
WO2019038060A1 (en) 2017-08-24 2019-02-28 Henkel Ag & Co. Kgaa DETERGENT COMPOSITION COMPRISING XANTHANE LYASE II VARIANTS
US11359188B2 (en) 2017-08-24 2022-06-14 Novozymes A/S Xanthan lyase variants and polynucleotides encoding same
WO2019057758A1 (en) 2017-09-20 2019-03-28 Novozymes A/S USE OF ENZYMES TO ENHANCE WATER ABSORPTION AND / OR WHITENESS
EP3684899A1 (en) 2017-09-22 2020-07-29 Novozymes A/S Novel polypeptides
CA3073362A1 (en) 2017-09-27 2019-04-04 Novozymes A/S Lipase variants and microcapsule compositions comprising such lipase variants
JP7114697B2 (ja) 2017-09-27 2022-08-08 ザ プロクター アンド ギャンブル カンパニー リパーゼを含む洗剤組成物
EP3692147A1 (en) 2017-10-02 2020-08-12 Novozymes A/S Polypeptides having mannanase activity and polynucleotides encoding same
MX2020003411A (es) 2017-10-02 2020-07-20 Novozymes As Polipeptidos que tienen actividad de mananasa y polinucleotidos que los codifican.
US20230193162A1 (en) 2017-10-16 2023-06-22 Novozymes A/S Low dusting granules
WO2019076800A1 (en) 2017-10-16 2019-04-25 Novozymes A/S CLEANING COMPOSITIONS AND USES THEREOF
US20200318037A1 (en) 2017-10-16 2020-10-08 Novozymes A/S Low dusting granules
EP3701001A1 (en) 2017-10-24 2020-09-02 Novozymes A/S Compositions comprising polypeptides having mannanase activity
PL3476936T3 (pl) 2017-10-27 2022-04-11 The Procter & Gamble Company Kompozycje detergentu zawierające odmiany polipeptydowe
WO2019081721A1 (en) 2017-10-27 2019-05-02 Novozymes A/S VARIANTS OF DNASE
DE102017125558A1 (de) 2017-11-01 2019-05-02 Henkel Ag & Co. Kgaa Reinigungszusammensetzungen, die dispersine i enthalten
DE102017125560A1 (de) 2017-11-01 2019-05-02 Henkel Ag & Co. Kgaa Reinigungszusammensetzungen, die dispersine iii enthalten
US11505767B2 (en) 2017-11-01 2022-11-22 Novozymes A/S Methods for cleansing medical devices
BR112020008711A2 (pt) 2017-11-01 2020-11-10 Novozymes A/S polipeptídeos e composições que compreendem tais polipeptídeos
US11767492B2 (en) 2017-11-01 2023-09-26 Novozymes A/S Methods of treating fabric using a Lactobacillus hexosaminidase
DE102017125559A1 (de) 2017-11-01 2019-05-02 Henkel Ag & Co. Kgaa Reinigungszusammensetzungen, die dispersine ii enthalten
EP3707255A1 (en) 2017-11-09 2020-09-16 Basf Se Coatings of enzyme particles comprising organic white pigments
BR112020010630A2 (pt) 2017-11-29 2020-11-10 Basf Se preparação de enzima líquida, processo para fabricar uma preparação de enzima, métodos para estabilizar pelo menos uma enzima e para remover manchas, e, formulação detergente.
CN111670248A (zh) 2017-12-04 2020-09-15 诺维信公司 脂肪酶变体以及编码其的多核苷酸
EP3749759A1 (en) 2018-02-08 2020-12-16 Novozymes A/S Lipase variants and compositions thereof
WO2019154951A1 (en) 2018-02-08 2019-08-15 Novozymes A/S Lipases, lipase variants and compositions thereof
EP3755793A1 (en) 2018-02-23 2020-12-30 Henkel AG & Co. KGaA Detergent composition comprising xanthan lyase and endoglucanase variants
WO2019175240A1 (en) 2018-03-13 2019-09-19 Novozymes A/S Microencapsulation using amino sugar oligomers
US11535837B2 (en) 2018-03-29 2022-12-27 Novozymes A/S Mannanase variants and polynucleotides encoding same
WO2019201793A1 (en) 2018-04-17 2019-10-24 Novozymes A/S Polypeptides comprising carbohydrate binding activity in detergent compositions and their use in reducing wrinkles in textile or fabric.
WO2019201783A1 (en) 2018-04-19 2019-10-24 Novozymes A/S Stabilized cellulase variants
CN118530973A (zh) 2018-04-19 2024-08-23 诺维信公司 稳定化的纤维素酶变体
CN112368375A (zh) 2018-04-26 2021-02-12 巴斯夫欧洲公司 脂肪酶
EP3788145A1 (en) 2018-05-03 2021-03-10 Basf Se Amylase enzymes
WO2019238761A1 (en) 2018-06-15 2019-12-19 Basf Se Water soluble multilayer films containing wash active chemicals and enzymes
EP3814472A1 (en) 2018-06-28 2021-05-05 Novozymes A/S Detergent compositions and uses thereof
EP3814473A1 (en) 2018-06-29 2021-05-05 Novozymes A/S Detergent compositions and uses thereof
EP3818139A1 (en) 2018-07-02 2021-05-12 Novozymes A/S Cleaning compositions and uses thereof
US20210301223A1 (en) 2018-07-03 2021-09-30 Novozymes A/S Cleaning compositions and uses thereof
WO2020008024A1 (en) 2018-07-06 2020-01-09 Novozymes A/S Cleaning compositions and uses thereof
WO2020030623A1 (en) 2018-08-10 2020-02-13 Basf Se Packaging unit comprising a detergent composition containing an enzyme and at least one chelating agent
WO2020070063A2 (en) 2018-10-01 2020-04-09 Novozymes A/S Detergent compositions and uses thereof
WO2020070209A1 (en) 2018-10-02 2020-04-09 Novozymes A/S Cleaning composition
CN112969775A (zh) 2018-10-02 2021-06-15 诺维信公司 清洁组合物
US20220073845A1 (en) 2018-10-02 2022-03-10 Novozymes A/S Endonuclease 1 ribonucleases for cleaning
WO2020070014A1 (en) 2018-10-02 2020-04-09 Novozymes A/S Cleaning composition comprising anionic surfactant and a polypeptide having rnase activity
EP3861008A1 (en) 2018-10-03 2021-08-11 Novozymes A/S Polypeptides having alpha-mannan degrading activity and polynucleotides encoding same
WO2020070249A1 (en) 2018-10-03 2020-04-09 Novozymes A/S Cleaning compositions
BR112021005412A2 (pt) 2018-10-05 2021-06-15 Basf Se preparação de enzima, processo para fabricar uma preparação de enzima estável, métodos para reduzir a perda da atividade proteolítica, para preparação de uma formulação detergente, para remover manchas e para aumentar a estabilidade na armazenagem de uma formulação detergente líquida, usos de um composto e da preparação de enzima, e, formulação detergente
WO2020069913A1 (en) 2018-10-05 2020-04-09 Basf Se Compounds stabilizing hydrolases in liquids
US20220112479A1 (en) 2018-10-05 2022-04-14 Basf Se Compounds stabilizing amylases in liquids
EP3677676A1 (en) 2019-01-03 2020-07-08 Basf Se Compounds stabilizing amylases in liquids
CN112996894A (zh) 2018-10-11 2021-06-18 诺维信公司 清洁组合物及其用途
EP3647398B1 (en) 2018-10-31 2024-05-15 Henkel AG & Co. KGaA Cleaning compositions containing dispersins v
EP3647397A1 (en) 2018-10-31 2020-05-06 Henkel AG & Co. KGaA Cleaning compositions containing dispersins iv
WO2020104231A1 (en) 2018-11-19 2020-05-28 Basf Se Powders and granules containing a chelating agent and an enzyme
BR112021009639A2 (pt) 2018-11-20 2021-09-28 Dupont Nutrition Biosciences Aps Polipeptídeos do clado tm-fitase alta robustos geneticamente modificados e fragmentos dos mesmos
EP3891264A1 (en) 2018-12-03 2021-10-13 Novozymes A/S LOW pH POWDER DETERGENT COMPOSITION
WO2020127796A2 (en) 2018-12-21 2020-06-25 Novozymes A/S Polypeptides having peptidoglycan degrading activity and polynucleotides encoding same
EP3898919A1 (en) 2018-12-21 2021-10-27 Novozymes A/S Detergent pouch comprising metalloproteases
MX2021010110A (es) 2019-02-20 2021-09-21 Basf Se Proceso de fermentacion industrial para bacillus mediante el uso de medio definido y alimentacion de magnesio.
US20220186234A1 (en) 2019-02-20 2022-06-16 Basf Se Industrial Fermentation Process for Bacillus Using Defined Medium and Trace Element Feed
CA3122942A1 (en) 2019-03-21 2020-09-24 Novozymes A/S Alpha-amylase variants and polynucleotides encoding same
EP3947619A1 (en) 2019-04-03 2022-02-09 Novozymes A/S Polypeptides having beta-glucanase activity, polynucleotides encoding same and uses thereof in cleaning and detergent compositions
CN113874499A (zh) 2019-04-10 2021-12-31 诺维信公司 多肽变体
CN113795576A (zh) 2019-04-12 2021-12-14 诺维信公司 稳定化的糖苷水解酶变体
WO2020229480A1 (en) 2019-05-14 2020-11-19 Basf Se Compounds stabilizing hydrolases in liquids
CN113993878A (zh) 2019-06-13 2022-01-28 巴斯夫欧洲公司 用二价阳离子从发酵液中回收蛋白的方法
EP3994148A1 (en) 2019-07-01 2022-05-11 Basf Se Peptide acetals for stabilising enzymes
WO2021001400A1 (en) 2019-07-02 2021-01-07 Novozymes A/S Lipase variants and compositions thereof
WO2021001297A1 (en) 2019-07-02 2021-01-07 Basf Se Method for preparing a fermentation medium
MX2022000253A (es) 2019-07-05 2022-02-03 Basf Se Proceso de fermentacion industrial para celulas microbianas mediante el uso de un precultivo de alimentacion por lotes.
CA3146541A1 (en) 2019-07-09 2021-01-14 Dupont Nutrition Biosciences Aps Fat coated particulate enzyme compositions
EP3997202A1 (en) 2019-07-12 2022-05-18 Novozymes A/S Enzymatic emulsions for detergents
WO2021030400A1 (en) 2019-08-13 2021-02-18 Novozymes Bioag A/S Pesticidal combinations of yersinia and proteases
US20220330576A1 (en) 2019-08-16 2022-10-20 Dupont Nutrition Biosciences Aps Compositions for gut health
US20220325204A1 (en) 2019-08-27 2022-10-13 Novozymes A/S Detergent composition
EP4022020A1 (en) 2019-08-27 2022-07-06 Novozymes A/S Composition comprising a lipase
WO2021046073A1 (en) 2019-09-05 2021-03-11 Dupont Nutrition Biosciences Aps Feed composition
CN114616312A (zh) 2019-09-19 2022-06-10 诺维信公司 洗涤剂组合物
WO2021064068A1 (en) 2019-10-03 2021-04-08 Novozymes A/S Polypeptides comprising at least two carbohydrate binding domains
BR112022006082A2 (pt) 2019-10-18 2022-06-21 Basf Se Preparação enzimática, formulação de detergente, e, uso de pelo menos um diol
EP4048081A2 (en) 2019-10-21 2022-08-31 DuPont Nutrition Biosciences ApS Compositions for gut health
US20230009832A1 (en) 2019-11-20 2023-01-12 Dupont Nutrition Biosciences Aps Thermostable phytase variants
WO2021105336A1 (en) 2019-11-29 2021-06-03 Basf Se Compositions comprising polymer and enzyme
WO2021115912A1 (en) 2019-12-09 2021-06-17 Basf Se Formulations comprising a hydrophobically modified polyethyleneimine and one or more enzymes
EP4076002A1 (en) 2019-12-19 2022-10-26 DuPont Nutrition Biosciences ApS Diet formulations
WO2021121394A1 (en) 2019-12-20 2021-06-24 Novozymes A/S Stabilized liquid boron-free enzyme compositions
WO2021122117A1 (en) 2019-12-20 2021-06-24 Henkel Ag & Co. Kgaa Cleaning composition coprising a dispersin and a carbohydrase
KR20220119607A (ko) 2019-12-20 2022-08-30 헨켈 아게 운트 코. 카게아아 디스페르신 ix를 포함하는 세정 조성물
EP4077656A2 (en) 2019-12-20 2022-10-26 Novozymes A/S Polypeptides having proteolytic activity and use thereof
CN114829562A (zh) 2019-12-20 2022-07-29 汉高股份有限及两合公司 包含分散蛋白vi的清洁组合物
EP4097206B1 (en) 2020-01-29 2023-08-09 Unilever IP Holdings B.V. Laundry detergent product
CN115052981A (zh) 2020-01-31 2022-09-13 诺维信公司 甘露聚糖酶变体以及编码它们的多核苷酸
EP4097226A1 (en) 2020-01-31 2022-12-07 Novozymes A/S Mannanase variants and polynucleotides encoding same
WO2021158927A1 (en) 2020-02-07 2021-08-12 Dupont Nutrition Biosciences Aps Feed compositions for animal health
CN115066495A (zh) 2020-02-14 2022-09-16 巴斯夫欧洲公司 甘露聚糖酶变体
CN115915956A (zh) 2020-02-28 2023-04-04 杜邦营养生物科学有限公司 饲料组合物
EP3892708A1 (en) 2020-04-06 2021-10-13 Henkel AG & Co. KGaA Cleaning compositions comprising dispersin variants
JP2023520312A (ja) 2020-04-08 2023-05-17 ノボザイムス アクティーゼルスカブ 炭水化物結合モジュールバリアント
WO2021214059A1 (en) 2020-04-21 2021-10-28 Novozymes A/S Cleaning compositions comprising polypeptides having fructan degrading activity
EP3907271A1 (en) 2020-05-07 2021-11-10 Novozymes A/S Cleaning composition, use and method of cleaning
US20230235250A1 (en) 2020-06-18 2023-07-27 Basf Se Compositions and Their Use
EP4172298A1 (en) 2020-06-24 2023-05-03 Novozymes A/S Use of cellulases for removing dust mite from textile
EP3936593A1 (en) 2020-07-08 2022-01-12 Henkel AG & Co. KGaA Cleaning compositions and uses thereof
US20230137116A1 (en) 2020-07-09 2023-05-04 Basf Se Compositions and their applications
WO2022008732A1 (en) 2020-07-10 2022-01-13 Basf Se Enhancing the activity of antimicrobial preservatives
CN116057158A (zh) 2020-07-27 2023-05-02 联合利华知识产权控股有限公司 酶和表面活性剂用于抑制微生物的用途
MX2023001888A (es) 2020-08-25 2023-03-10 Novozymes As Variantes de una xiloglucanasa de la familia 44.
EP4213641A1 (en) 2020-09-15 2023-07-26 Novozymes A/S Animal feed comprising insects or insect meal
CN116507725A (zh) 2020-10-07 2023-07-28 诺维信公司 α-淀粉酶变体
EP4228425A1 (en) 2020-10-16 2023-08-23 DuPont Nutrition Biosciences ApS Feed compositions for animal health
EP4232539A2 (en) 2020-10-20 2023-08-30 Novozymes A/S Use of polypeptides having dnase activity
WO2022083949A1 (en) 2020-10-20 2022-04-28 Basf Se Compositions and their use
EP4237525A1 (en) 2020-10-28 2023-09-06 Novozymes A/S Use of lipoxygenase
US20240035005A1 (en) 2020-10-29 2024-02-01 Novozymes A/S Lipase variants and compositions comprising such lipase variants
EP4244325A1 (en) 2020-11-13 2023-09-20 Novozymes A/S Detergent composition comprising a lipase
WO2022106400A1 (en) 2020-11-18 2022-05-27 Novozymes A/S Combination of immunochemically different proteases
EP4032966A1 (en) 2021-01-22 2022-07-27 Novozymes A/S Liquid enzyme composition with sulfite scavenger
US20240124805A1 (en) 2021-01-28 2024-04-18 Novozymes A/S Lipase with low malodor generation
WO2022169933A2 (en) 2021-02-03 2022-08-11 Dupont Nutrition Biosciences Aps Compositions for gut health
EP4039806A1 (en) 2021-02-04 2022-08-10 Henkel AG & Co. KGaA Detergent composition comprising xanthan lyase and endoglucanase variants with im-proved stability
WO2022171872A1 (en) 2021-02-12 2022-08-18 Novozymes A/S Stabilized biological detergents
WO2022171780A2 (en) 2021-02-12 2022-08-18 Novozymes A/S Alpha-amylase variants
US20240301328A1 (en) 2021-03-12 2024-09-12 Novozymes A/S Polypeptide variants
US20240060061A1 (en) 2021-03-15 2024-02-22 Novozymes A/S Dnase variants
EP4060036A1 (en) 2021-03-15 2022-09-21 Novozymes A/S Polypeptide variants
CN117083370A (zh) 2021-03-26 2023-11-17 诺维信公司 聚合物含量降低的洗涤剂组合物
EP4359518A1 (en) 2021-06-23 2024-05-01 Novozymes A/S Alpha-amylase polypeptides
CA3232987A1 (en) 2021-09-27 2023-03-30 Marion BERNARDEAU Feed additive compositions and methods for using the same
EP4416256A1 (en) 2021-10-13 2024-08-21 Basf Se Compositions comprising polymers, polymers, and their use
WO2023066741A1 (en) 2021-10-20 2023-04-27 Basf Se Phosphate-free composition and methods for their manufacture and use
MX2024006197A (es) 2021-11-22 2024-06-11 Basf Se Composiciones que comprenden polimeros, polimeros y su uso.
WO2023088776A1 (en) 2021-11-22 2023-05-25 Basf Se Compositions comprising polymers, polymers, and their use
CN118401646A (zh) 2021-12-17 2024-07-26 巴斯夫欧洲公司 组合物及其应用
WO2023116569A1 (en) 2021-12-21 2023-06-29 Novozymes A/S Composition comprising a lipase and a booster
WO2023117936A1 (en) 2021-12-21 2023-06-29 Basf Se Environmental attributes for chemical compounds comprising a carbonyl group
EP4206309A1 (en) 2021-12-30 2023-07-05 Novozymes A/S Protein particles with improved whiteness
EP4234664A1 (en) 2022-02-24 2023-08-30 Evonik Operations GmbH Composition comprising glucolipids and enzymes
CN118660951A (zh) 2022-03-02 2024-09-17 诺维信公司 木葡聚糖酶用于改善洗涤剂的可持续性的用途
AU2023228020A1 (en) 2022-03-04 2024-07-11 Novozymes A/S Dnase variants and compositions
WO2023194204A1 (en) 2022-04-08 2023-10-12 Novozymes A/S Hexosaminidase variants and compositions
WO2023233028A1 (en) 2022-06-03 2023-12-07 Unilever Ip Holdings B.V. Laundry detergent product
WO2023247348A1 (en) 2022-06-21 2023-12-28 Novozymes A/S Mannanase variants and polynucleotides encoding same
WO2023247664A2 (en) 2022-06-24 2023-12-28 Novozymes A/S Lipase variants and compositions comprising such lipase variants
WO2024012894A1 (en) 2022-07-15 2024-01-18 Basf Se Alkanolamine formates for enzyme stabilization in liquid formulations
WO2024083589A1 (en) 2022-10-18 2024-04-25 Basf Se Detergent compositions, polymers and methods of manufacturing the same
WO2024121057A1 (en) 2022-12-05 2024-06-13 Novozymes A/S A composition for removing body grime
WO2024124013A1 (en) 2022-12-09 2024-06-13 International N&H Denmark Aps Feed formulations comprising a phytase for dairy ruminant animals
WO2024126483A1 (en) 2022-12-14 2024-06-20 Novozymes A/S Improved lipase (gcl1) variants
EP4389864A1 (en) 2022-12-20 2024-06-26 Basf Se Cutinases
WO2024131880A2 (en) 2022-12-23 2024-06-27 Novozymes A/S Detergent composition comprising catalase and amylase
WO2024156628A1 (en) 2023-01-23 2024-08-02 Novozymes A/S Cleaning compositions and uses thereof

Citations (10)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1987005050A1 (en) * 1986-02-12 1987-08-27 Genex Corporation Mutagenesis and screening method and product
EP0236040A2 (en) * 1986-02-26 1987-09-09 Collaborative Research Inc. Amino acid modified prourokinase and method of preparation
WO1989001520A1 (en) * 1987-08-11 1989-02-23 Cetus Corporation Procaryotic xylose isomerase muteins and method to increase protein stability
WO1989009819A1 (en) * 1988-04-12 1989-10-19 Genex Corporation Combining mutations for stabilization of subtilisin
US4980288A (en) * 1986-02-12 1990-12-25 Genex Corporation Subtilisin with increased thermal stability
WO1991000345A1 (en) * 1989-06-26 1991-01-10 Novo Nordisk A/S A mutated subtilisin protease
US5185258A (en) * 1984-05-29 1993-02-09 Genencor International, Inc. Subtilisin mutants
US5324653A (en) * 1988-02-11 1994-06-28 Gist-Brocades N.V. Recombinant genetic means for the production of serine protease muteins
US5336611A (en) * 1988-02-11 1994-08-09 Gist-Brocades N.V. PB92 serine protease muteins and their use in detergents
US5340735A (en) * 1991-05-29 1994-08-23 Cognis, Inc. Bacillus lentus alkaline protease variants with increased stability

Patent Citations (10)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5185258A (en) * 1984-05-29 1993-02-09 Genencor International, Inc. Subtilisin mutants
WO1987005050A1 (en) * 1986-02-12 1987-08-27 Genex Corporation Mutagenesis and screening method and product
US4980288A (en) * 1986-02-12 1990-12-25 Genex Corporation Subtilisin with increased thermal stability
EP0236040A2 (en) * 1986-02-26 1987-09-09 Collaborative Research Inc. Amino acid modified prourokinase and method of preparation
WO1989001520A1 (en) * 1987-08-11 1989-02-23 Cetus Corporation Procaryotic xylose isomerase muteins and method to increase protein stability
US5324653A (en) * 1988-02-11 1994-06-28 Gist-Brocades N.V. Recombinant genetic means for the production of serine protease muteins
US5336611A (en) * 1988-02-11 1994-08-09 Gist-Brocades N.V. PB92 serine protease muteins and their use in detergents
WO1989009819A1 (en) * 1988-04-12 1989-10-19 Genex Corporation Combining mutations for stabilization of subtilisin
WO1991000345A1 (en) * 1989-06-26 1991-01-10 Novo Nordisk A/S A mutated subtilisin protease
US5340735A (en) * 1991-05-29 1994-08-23 Cognis, Inc. Bacillus lentus alkaline protease variants with increased stability

Non-Patent Citations (30)

* Cited by examiner, † Cited by third party
Title
Balajai et al., Biochem. Biophys. Research Comm. vol. 160, No. 1, 109 14 (1989). *
Balajai et al., Biochem. Biophys. Research Comm. vol. 160, No. 1, 109-14 (1989).
Estink, M.R., et al., 1990, Proceedings of the SPIE International Society of Optical Engineers, 10241(2Pt.1): 137 143. *
Estink, M.R., et al., 1990, Proceedings of the SPIE International Society of Optical Engineers, 10241(2Pt.1): 137-143.
Jacobs et al., Nucleic Acid Research, vol. 13, No. 24, pp. 8913 8926. *
Jacobs et al., Nucleic Acid Research, vol. 13, No. 24, pp. 8913-8926.
Jany et al., Biol. Chem. Hoppe Seyler, vol. 366, pp. 485 492 (1985). *
Jany et al., Biol. Chem. Hoppe-Seyler, vol. 366, pp. 485-492 (1985).
Kurihara et al., J. Biological Chem., vol. 247, No. 17, pp. 5619 5631 (1985). *
Kurihara et al., J. Biological Chem., vol. 247, No. 17, pp. 5619-5631 (1985).
Meloun et al., FEBS Letters 2463, vol. 183, No. 2, pp. 195 200 (1985). *
Meloun et al., FEBS Letters 2463, vol. 183, No. 2, pp. 195-200 (1985).
Nedkov et al., Biol. Chem. Hoppe Seyler, vol. 366, pp. 421 430 (1985). *
Nedkov et al., Biol. Chem. Hoppe-Seyler, vol. 366, pp. 421-430 (1985).
Piela et al., Biopolymers, vol. 26, pp. 1587 1600 (1987). *
Piela et al., Biopolymers, vol. 26, pp. 1587-1600 (1987).
Priest, Bacteriological Reviews, vol. 41, No. 3, pp. 711 753 (1977). *
Priest, Bacteriological Reviews, vol. 41, No. 3, pp. 711-753 (1977).
Svendsen et al., FEBS Letters 3361, vol. 196, No. 2, pp. 228 232 (1986). *
Svendsen et al., FEBS Letters 3361, vol. 196, No. 2, pp. 228-232 (1986).
Takagi, H., et al., 1989, Journal of Biochemistry, 105(6): 953 956. *
Takagi, H., et al., 1989, Journal of Biochemistry, 105(6): 953-956.
Vasantha et al., J. Bacteriology, vol. 159, No. 3, pp. 811 819 (1984). *
Vasantha et al., J. Bacteriology, vol. 159, No. 3, pp. 811-819 (1984).
Wells et al., Nucleic Acids Research, vol. 11, No. 22, pp. 7911 925 (1983). *
Wells et al., Nucleic Acids Research, vol. 11, No. 22, pp. 7911-925 (1983).
White et al. Principles of Biochemistry, Fifth Edition, pp. 271 272 (1973). *
White et al. Principles of Biochemistry, Fifth Edition, pp. 271-272 (1973).
Wu, H. et al., 1990, Proceedings of the National Academy of Sciences, U.S.A., 87:5888 5892. *
Wu, H. et al., 1990, Proceedings of the National Academy of Sciences, U.S.A., 87:5888-5892.

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